Peters Plus Syndrome Is a New Congenital Disorder of Glycosylation and Involves Defective O-Glycosylation of Thrombospondin Type 1 Repeats*
نویسندگان
چکیده
Daniel Hess, Jeremy J. Keusch, Saskia A. Lesnik Oberstein, Raoul C. M. Hennekam , and Jan Hofsteenge From the Friedrich Miescher Institute for Biomedical Research, Basel CH-4058, Switzerland, the Center for Human and Clinical Genetics, Department of Clinical Genetics, K5-R, Leiden University Medical Center, 2300 RC Leiden, The Netherlands, the Clinical and Molecular Genetics Unit, Institute of Child Health, London WC1N 3JH, United Kingdom, and the Department of Pediatrics, Academic Medical Center, 1105 AZ Amsterdam, The Netherlands
منابع مشابه
Peters Plus syndrome is a new congenital disorder of glycosylation and involves defective Omicron-glycosylation of thrombospondin type 1 repeats.
Peters Plus syndrome is an autosomal recessive disorder characterized by anterior eye chamber defects, disproportionate short stature, developmental delay, and cleft lip and/or palate. It is caused by splice site mutations in what was thought to be a beta1,3-galactosyltransferase-like gene (B3GALTL). Recently, we and others found this gene to encode a beta1,3-glucosyltransferase involved in the...
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BACKGROUND O-fucose is added to cysteine-rich domains called thrombospondin type 1 repeats (TSRs) by protein O-fucosyltransferase 2 (POFUT2) and is elongated with glucose by β3-glucosyltransferase (B3GLCT). Mutations in B3GLCT result in Peters plus syndrome (PPS), an autosomal recessive disorder characterized by eye and other developmental defects. Although 49 putative targets are known, the fu...
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Peters Plus syndrome (PPS), a congenital disorder of glycosylation, results from recessive mutations affecting the glucosyltransferase B3GLCT, leading to congenital corneal opacity and diverse extra-ocular manifestations. Together with the fucosyltransferase POFUT2, B3GLCT adds Glucoseβ1-3Fucose disaccharide to a consensus sequence in thrombospondin type 1 repeats (TSRs) of several proteins. Wh...
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Glycosylation is the most frequent modification of proteins and is important for many ligand-receptor interactions. Recently, defects in protein glycosylation have been linked to several forms of congenital muscular dystrophy that are frequently associated with brain abnormalities. Muscle-eye-brain disease and Walker-Warburg syndrome are caused by mutations in enzymes involved in O-mannosylatio...
متن کاملCongenital disorders of glycosylation. Part II. Defects of protein O-glycosylation.
Glycosylation is a form of post-translational modification of proteins and occurs in every living cell. The carbohydrate chains attached to the proteins serve various functions. There are two main types of protein glycosylation: N-glycosylation and O-glycosylation. In this paper, we describe the O-glycosylation process and currently known congenital disorders of glycosylation associated with de...
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تاریخ انتشار 2008